Biochip substrate and biochip
a technology of biochips and substrates, applied in the field of biochips, can solve the problems of high cost, difficult stabilization and synthesis of long oligonucleotides, and variability in the amount of immobilized molecules
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example 1
1. Production of Substrate for Biochips (Part 1)
[0025]A high purity Al—Mg alloy plate (Mg content: 4% by weight) with a thickness of 1.2 mm was sized to 26 mm×76 mm by punching with a press. A plurality of the plates were stacked and annealed under pressure under an atmosphere at 340° C., thereby removing strain and attaining a flatness of not more than 5 μm. Thereafter, working of the end faces and chamfer (specifically, angle 45°, a length: 0.2 mm) was performed to prepare plates with a size of 25 mm×75 mm. Then each plate was ground with a double side grinding machine 16B produced by SpeedFam, in which a sponge grindstone was mounted, to attain a thickness of 0.98 mm and a degree of parallelization of not more than 1 μm. Then micro recesses with a size shown in FIG. 1 were formed in the substrate by mechanical processing with a microdrill using a marking press CAMM-3 produced by Roland. The resulting plate was then subjected to, in the order mentioned, degreasing, etching, acid a...
example 2
2. Production of Substrate for Biochips (Part 2)
[0027]After placing a thermosetting phenol resin in a mold, a two-step heat treatment at 90° C. and 120° C. was performed to prepare a Bakelite block. A plate having a thickness of 2 mm and a size of 31 mm×95 mm was cut out from the block, and was ground with a double side polishing machine 16B produced by SpeedFam, in which an iron surface plate was mounted, to attain a thickness of 1.30 mm and a degree of parallelization of not more than 1 μm. After chamfering, the resulting plate was slowly heated to 1200° C. thereby carbonizing the substrate to amorphous carbon. Thereafter, using a LD-excited YVO4 laser produced by Fuji Electric, the small recesses having the size shown in FIG. 1 were formed in the air, and then functional groups were attached by the following method: First, the substrate was set in a stainless steel vessel having a window made of a synthetic quartz, and irradiated with an ultraviolet lamp (lamp output power: 110 W...
example 3
[0028]Calmodulin was measured using a peptide chip having recesses in which a peptide having α-helix structure was immobilized, which peptide was labeled with different fluorescence labels at its both ends. More specifically, this was carried out as follows:
[0029]The sequence of the core region of the peptide having α-helix structure was designed by molecular modeling using a computer (molecular modeling using Insight II / Discover of Molecular Simulation, U.S.) based on the amino acid sequence of the peptide described in a reference (K. T. O'Neil and W. F. DeGrado, Trend Biochem Sci, 15, 59-64 (1990)). As a result, the designed amino acid sequence of the core region was Leu-Lys-Lys-Leu-Leu-Lys-Leu-Leu-Lys-Lys-Leu-Leu-Lys-Leu (SEQ ID NO:1). This sequence is known to specifically bind to calmodulin. To this sequence, a Cys residue as an anchor for immobilization, and as fluorescently labeled residues, Lys(TAMRA) and Lys(FAM) were added. Thus, an amino acid sequence Cys-Lys(TAMRA)-Leu-L...
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